PDBsum entry 4y6c

Unknown function

PDB id: 4y6c

Contents

Protein chain

212 a.a.

Ligands

SO4 ×2

Waters ×169

PDB id:

4y6c

Name:

Unknown function

Title:

Q17m crystal structure of podosopora anserina putative kinesin light chain nearly identical tpr-like repeats

Structure:

Anserina putative kinesin light chain. Chain: a. Synonym: q17m. Engineered: yes

Source:

Podospora anserina. Organism_taxid: 5145. Strain: s mat+. Gene: cdp31375.1. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: rosetta 2.

Resolution:

1.77Å R-factor: 0.175 R-free: 0.214

Authors:

J.D.Marold,J.M.Kavran,G.D.Bowman,D.Barrick

Key ref:

J.D.Marold et al. (2015). A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins. Structure, 23, 2055-2065. PubMed id: 26439765 DOI: 10.1016/j.str.2015.07.022

Date:

12-Feb-15 Release date: 07-Oct-15

Protein chain

A0A090CRQ5  (A0A090CRQ5_PODAN) -  Kinesin light chain from Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)

Seq: 1067 a.a.

Struc: 212 a.a.*

* PDB and UniProt seqs differ at 30 residue positions (black crosses)

DOI no: 10.1016/j.str.2015.07.022

Structure 23:2055-2065 (2015)

PubMed id: 26439765

A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.

J.D.Marold, J.M.Kavran, G.D.Bowman, D.Barrick.

ABSTRACT

Linear repeat proteins often have high structural similarity and low (∼25%) pairwise sequence identities (PSI) among modules. We identified a unique P. anserina (Pa) sequence with tetratricopeptide repeat (TPR) homology, which contains longer (42 residue) repeats (42PRs) with an average PSI >91%. We determined the crystal structure of five tandem Pa 42PRs to 1.6 Å, and examined the stability and solution properties of constructs containing three to six Pa 42PRs. Compared with 34-residue TPRs (34PRs), Pa 42PRs have a one-turn extension of each helix, and bury more surface area. Unfolding transitions shift to higher denaturant concentration and become sharper as repeats are added. Fitted Ising models show Pa 42PRs to be more cooperative than consensus 34PRs, with increased magnitudes of intrinsic and interfacial free energies. These results demonstrate the tolerance of the TPR motif to length variation, and provide a basis to understand the effects of helix length on intrinsic/interfacial stability.